PBB geneid 4151 Myoglobin is an iron and oxygen binding protein found in the muscle tissue of vertebrates ... binding protein in blood, specifically in the red blood cells. The only time myoglobin is found in the bloodstream ... 2000 page 206 edition 3rd isbn 071676203X ref Myoglobin abbreviated Mb is a tertiary structure single ... pigment pigment of muscle tissues. ref name review cite journal title Myoglobin an essential hemoprotein ... http www.ncbi.nlm.nih.gov entrez query.fcgi?cmd Search&db books&doptcmdl GenBookHL&term myoglobin ... protein family members myoglobin and hemoglobin title Molecular Cell Biology edition 4th author ... proteins only. Instead, the binding of oxygen by myoglobin is unaffected by the oxygen pressure in the surrounding tissue. Myoglobin is often cited as having an instant binding tenacity to oxygen given its hyperbolic oxygen Dissociation chemistry dissociation curve. High concentrations of myoglobin ... have muscles with particularly high myoglobin abundance. ref name Nelson00 Myoglobin was the first ... 3.17.2010 ref In 1958, John Kendrew and associates successfully determined the structure of myoglobin ... Model of the Myoglobin Molecule Obtained by X Ray Analysis author JC Kendrew, G Bodo, HM Dintzis ... genetically engineered to lack myoglobin are viable, but showed a 30 reduction in cardiac systolic .... ref name mice cite journal title Hypoxia induced left ventricular dysfunction in myoglobin deficient ... 41 pmid 12881221 issue 5 doi 10.1152 ajpheart.00147.2003 ref In humans myoglobin is encoded by the MB gene . ref name pmid2989088 cite journal author Akaboshi E title Cloning of the human myoglobin ... myoglobinMyoglobin forms pigment s responsible for making meat red meat red . The color that meat takes is partly determined by the oxidation states of the iron atom in myoglobin and the oxygen species ... 31, 2007 http www.startribune.com 535 story 1518775.html ref Myoglobin is found in Type I muscle, Type II A and Type II B, but most texts consider myoglobin not to be found in smooth muscle. Role in disease ... more details
Orphan date February 2009 A coboglobin is a synthetic compound, a metalloprotein chemically similar to hemoglobin or myoglobin but using the metal cobalt instead of iron hence the name . Just like hemoglobin and myoglobin, the coboglobins are able to reversibly bind molecular oxygen O sub 2 sub at the metal atom. However they lose this ability much faster than the natural molecules . Blood of this type would be amber yellow in colour when in the veins while uncoloured and clear in the arteries . References B. M. Hoffman, D. H. Petering. Coboglobins Oxygen Carrying Cobalt Reconstituted Hemoglobin and Myoglobin. Proceedings of the National Academy of Sciences of the United States of America , Vol. 67, No. 2 Oct. 15, 1970 , pp. 637 643 Category Metalloproteins ru ... more details
Infobox disease Name Myoglobinuria Image RhabdoUrine.JPG Caption Urine from a person with rhabdomyolysis showing the characteristic brown discoloration as a result of myoglobinuria DiseasesDB 23059 ICD10 ICD10 R 82 1 r 80 ICD9 ICD9 791.3 ICDO OMIM MedlinePlus eMedicineSubj ped eMedicineTopic 1535 MeshID D009212 File Myoglobin.png thumb Model of helical domains in myoglobin. Myoglobinuria is the presence of myoglobin in the urine , usually associated with rhabdomyolysis or muscle destruction. Myoglobin is present in muscle cells as a reserve of oxygen . Causes Physical trauma Trauma , vascular problems, venom s, certain drugs and other situations can destroy or damage the muscle, releasing myoglobin to the circulation and thus to the kidneys. Under ideal situations myoglobin will be filtered and excreted with the urine, but if too much myoglobin is released into the circulation or in case of renal problems, it can occlude the renal filtration system leading to acute tubular necrosis and acute renal insufficiency . Other causes of myoglobinuria include McArdle s disease Phosphofructokinase deficiency ref name pmid18421897 cite journal author Toscano A, Musumeci O title Tarui disease and distal glycogenoses clinical and genetic update journal Acta Myol volume 26 issue 2 pages 105 7 year 2007 month October pmid 18421897 doi url pmc 2949577 ref Carnitine palmitoyltransferase II deficiency Diagnosis After centrifuging, the serum of myoglobinuria is clear, where the serum of hemoglobinuria after centrifuge is pink. Citation needed date January 2008 External links http neuromuscular.wustl.edu msys myoglob.html Overview on the Neuromuscular disease center website. References reflist Abnormal clinical and laboratory findings for urine Category Abnormal clinical and laboratory findings for urine disease stub de Myoglobinurie ru ... more details
Metmyoglobin is the oxidised form of the oxygen carrying protein myoglobin . Metmyoglobin is the cause of the characteristic brown colouration of meat that occurs as it ages. In living muscle , the concentration of metmyoglobin is vanishingly small, due to the presence of the enzyme metmyoglobin reductase , which, in the presence of the Cofactor biochemistry cofactor NADH and the coenzyme cytochrome b4 converts the Iron Fe sup 3 sup in the heme heme prosthetic group of metmyoglobin back to the Fe sup 2 sup of normal myoglobin. In meat, which is dead muscle , the normal processes of removing metmyoglobin are prevented from effecting this repair, or alternatively the rate of metmyoglobin formation exceeds their capacity, so that there is a net accumulation of metmyoglobin as the meat ages. External links MeshName Metmyoglobin Globins Category Hemoproteins protein stub de Metmyoglobin ja ... more details
Unreferenced date August 2007 A meat slurry , reconstituted meat , or emulsified meat is a liquefied meat product that contains fewer fats, pigments and less myoglobin than unprocessed dark meat s. Meat slurry also eases the process of meat distribution and is more malleable than dark meats. Meat slurry is not designed to sell for general consumption rather, it is used as a meat supplement in food products for humans, such as chicken nuggets , and food for domestic animals. Poultry is the most common meat slurry however, beef and pork are also used. Properties and production Dark meat from poultry s characteristics, its color, low plasticity and high fat content, are caused by myoglobin , a pigmented chemical compound found in muscle tissue that undergoes frequent use. Because domestic poultry rarely fly, the flight muscles in the breast contain little myoglobin and appear white. Dark meat which is high in myoglobin is less useful in industry, especially fast food , because it is difficult to mold into shapes. Processing dark meat into a slurry makes it more like white meat, easier to prepare and more attractive. The meat is first finely ground and mixed with water. The mixture is then used in a centrifuge or with an emulsifier to separate the fats and myoglobin from the muscle. The product is then allowed to settle into three layers meat, excess water, and fat. The remaining liquefied meat is then Flash freezing flash frozen and packaged. See also Mechanically separated meat Offal External links http www.uga.edu news artman publish 050809fletcher.shtml UGA scientist takes dark out of chicken meat http news.bbc.co.uk 1 hi education 4287712.stm BBC News Junk Food to be Banned in Schools Category Meat Category Fast food Category Meat industry de Formfleisch ... more details
Other uses P50 disambiguation In biochemistry , P sub 50 sub indicates the partial pressure of a gas required to achieve 50 enzyme saturation. ref http medical dictionary.thefreedictionary.com P 50 ref ref http www.lexingtonpulmonary.com education oxyhb oxyhb.html ref Values of P sub 50 sub are negatively correlated with substrate affinity, with lower values of P sub 50 sub corresponding to high affinity and vice versa . The term is analogous to the Michaelis Menten constant K sub m sub , which identifies the concentration of substrate required for an enzyme to achieve 50 of its maximum enzyme reaction rate reaction velocity . For example, the P sub 50 sub of myoglobin for oxygen O sub 2 sub is 130 pascal unit pascal s while the P sub 50 sub for hemoglobin adult hemoglobin is 3.5 kPa. Thus, when O sub 2 sub partial pressure is low, hemoglobin bound O sub 2 sub is more readily transferred to myoglobin. Myoglobin, found in high concentrations in muscle tissue, can then transfer the oxygen to muscle fiber s, where it will be used in the generation of energy to fuel muscle contraction. ref cite journal pmid 2706089 ref References Reflist DEFAULTSORT P50 Pressure Category Enzyme kinetics Category Units of pressure biochem stub fr P50 ... more details
including Oxygen transport hemoglobin myoglobin neuroglobin cytoglobin leghemoglobin Catalysis ... Biological defense Defense catalase Hemoglobin and Myoglobin Hemoglobin and Myoglobin are examples of hemeprotein ... Hemoglobin is a quaternary protein that occurs in the red blood cell, whereas, myoglobin is a tertiary ... F8 of the myoglobin, also known as the proximal histadine is covalently bonded to the 5th coordination ... histidine a histidine that doesn t bond directly with the Iron , His E7 of the myoglobin binds ... more details
Synzymes are substances with catalytic capabilities. The name synzyme is derived from synthetic enzyme . Current synzymes consist mainly of organic molecules tailored in such a way that they catalyse certain kinds of reactions. Like enzymes, they bind a transition state of a substrate in an acitve site, and like enzymes they generally obey Michaelis Menten kinetics . Derivatised proteins If Ru NH sub 3 sub sub 5 sub sup 3 sup is attached to certain histidine residues in a myoglobin protein, myoglobin is no longer a passive oxygen carrier, but gains enzmatic activity of an oxidase . Ascorbic acid is oxidised with molecular oxygen. Antibodies can act as enzymes, then named abzyme s, if they are selected against transition state analogues. Abzymes have a low K sub M sub , meaning that they readily bind a target molecule, but have low V sub max sub values, indicating a slow reaction rate. Synzymes from organic molecules Cyclodextrins are cap structures with a hydrophilic exterior but a hydrophobic interior. If pyridoxal is anchored in the interior the cyclodextran shows transaminase activity. See also Enzyme Abzyme Catalysis References Wiseman A. Designer enzyme and cell applications in industry and in environmental monitoring. J Chem Technol Biotechnol. 1993 56 1 3 13 Diekmann S. et al. Metal mediated reactions modeled after nature. J Biotechnol. 2002 Apr 90 2 73 94 External links http www.lsbu.ac.uk biology enztech artificial.html enzyme stub Category Enzymes ... more details
Image Myoglobin 1mba.png thumb 300px An example of the globin fold, the oxygen carrying protein myoglobin PDB ID 1MBA from the mollusc Aplysia limacina . The globin fold is a common three dimensional tertiary structure fold in protein s. This fold typically consists of eight ref Aplysia limacina myoglobin. Crystallographic analy... J Mol Biol. 1989 PubMed result , n.d. http www.ncbi.nlm.nih.gov pubmed 2926816. ref alpha helix alpha helices , although some proteins have additional helix extensions at their termini. The globin fold is found in its namesake proteins hemoglobin and myoglobin as well as in phycocyanin proteins. Because myoglobin was the first protein whose structure was solved, the globin fold was thus the first protein fold discovered. Since the globin fold contains only helices, it is classified as an all alpha protein fold . Helix packing The eight helices of the globin fold core share significant nonlocal structure, unlike other structural motif s in which amino acid s close to each other in primary sequence are also close in space. The helices pack together at an average angle of about 50 degrees, significantly steeper than other helical packings such as the helix bundle . The exact angle of helix packing depends on the sequence of the protein, because packing is mediated by the steric s and hydrophobic interactions of the amino acid side chain s near the helix interfaces. Sequence conservation Although the globin fold is highly evolution arily Conserved sequence conserved , the sequences that form the fold can have as low as 16 sequence identity. While the sequence specificity of the fold is not stringent, the hydrophobic core of the protein must be maintained and hydrophobic patches on the generally hydrophilic solvent exposed surface must be avoided in order for the structure to remain stable and soluble . The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates ... more details
Multiple issues wikify February 2012 dead end February 2012 cleanup October 2009 Chromoprotein A conjugated protein, sulch as hemoglobin, that contains a pigmented prosthetic group, such as hem in hemoglobin which makes blood red . Other examples of chromoprotein are myoglobin, cytochromes and flavoproteins. In hemoglobin chromoprotein tetramer MW 4 x 16.125 64.500 Hem Fe four pyrrol rings. Category Carotenoids Category Hemoproteins Category Pigments Category Proteins protein stub ca Cromoprote na de Chromoproteine mk pl Chromoproteiny ru uk zh ... more details
pigments. Respiration Physiology 57 201 211. ref MyoglobinMyoglobin is an oxygen transport protein used in muscles, but is also absent from all icefish skeletal muscles. In ten species, myoglobin .... Costello. 1997. Variable expression of myoglobin among the hemoglobinless antarctic icefishes. Proceedings of the National Academy of Sciences of the United States of America 94 3420 3424. ref Myoglobin ... of hemoglobin and myoglobin expression in antarctic icefishes. Journal of Experimental Biology 209 ... more details
a Reader at the Davy Faraday Laboratory of the Royal Institution in London . Crystal structure of myoglobin File KendrewMyoglobin.jpg thumb 300px John Kendrew with model of myoglobin in progress. Copyright ... . Kendrew determined the structure of the protein myoglobin , which stores oxygen in muscle ... as far as was possible using the resources then available, Kendrew embarked on the study of myoglobin ... encounter led to his acquiring a large chunk of whale meat from Peru. Whale myoglobin did give ... myoglobin. Comparison between the amino acid sequences of sperm whale myoglobin and of human hemoglobin ... journal pmid 13672267 year 1959 month Jul last1 Kendrew first1 JC title Structure and function in myoglobin ... model of the myoglobin molecule obtained by x ray analysis volume 181 issue 4610 pages 662 6 issn 0028 ... title Orientation of the haem group in myoglobin and its relation to the polypeptide chain direction ... last2 Parris title Imidazole complexes of myoglobin and the position of the haem group volume 175 issue ... Marrack last4 Orlans title The species specificity of myoglobin volume 174 issue 4438 pages 946 9 issn ... more details
unreferenced date August 2009 Infobox Anatomy Name PAGENAME Latin sarcoplasma GraySubject GrayPage Image Musclon2.jpg Caption Muscle system Image2 Caption2 Precursor System Artery Vein Nerve Lymph MeshName MeshNumber Code TerminologiaHistologica 2 00 05.0.00004 The Sarcoplasm of a muscle fiber is comparable to the cytoplasm of other cells, but it houses unusually large amounts of glycosomes granules of stored glycogen and significant amounts of myoglobin , an oxygen binding protein. The calcium concentration in sarcoplasma is also a special element of the muscular fiber by means of which the contractions takes place and regulates. Other than the fact that it contains mostly myofibrils which are composed of sarcomere s , its contents are otherwise comparable to those of the cytoplasm of other cells. It has a Golgi apparatus , near the Cell nucleus nucleus , mitochondria just on the inside of the cytoplasmic membrane or sarcolemma , as well as a smooth endoplasmic reticulum organized in an extensive network. External links eMedicineDictionary sarcoplasm http medical.merriam webster.com medical sarcoplasm Merriam Webster Dictionary http www.encyclopedia.com doc 1O8 sarcoplasm.html Sarcoplasm at Encyclopedia.com br br Muscle tissue Category Cell anatomy cy Sarcoplasm es Sarcoplasma io Sarkoplasmo kk nl Sarcoplasma ja pl Sarkoplazma pt Sarcoplasma ru vi C t ng ... more details
This is a table of permselectivity for different substances in the glomerulus of the kidney in renal filtration . class wikitable Substance Molecular mass ref name boron cite book author Walter F. Boron, Emile L. Boulpaep title Medical Physiology A Cellular And Molecular Approach publisher Elsevier Saunders location year pages isbn 1 4160 2328 3 oclc doi Page 761 ref Effective molecular radius Nanometre nm ref name boron Concentration conc. in ultrafiltrate BR conc. in blood plasma ref name boron sodium 23 0.1 1.0 potassium 39 0.14 1.0 chloride 35,5 0.18 1.0 water 18 0.15 1.0 urea 60 0.16 1.0 glucose 180 0.33 1.0 sucrose 342 0.44 1.0 polyethylene glycol 1.000 0.70 1.0 inulin 5.200 1.48 0.98 lysozyme 14.600 1.90 0.8 myoglobin 16.900 1.88 0.75 lactoglobulin 36.000 2.16 0.4 egg albumin 43.500 2.80 0.22 Bence Jones protein 44.000 2.77 1.0 hemoglobin 68.000 3.25 0.03 serum albumin 69.000 3.55 0.01 References references renal physiology Category Physiology ... more details
by dissection of Hoyle s argument made in relation to myoglobin . ref Evolution from Space 1982 ... and v different values at each position of v sup n sup possibilities. Therefore myoglobin, a protein ... analysis must consider the smallest such space that contains a functional myoglobin. Neither n 153 nor v 20 can be accepted as minimal requirements, a priori. Myoglobin function is in fact a property ... a functional myoglobin cannot be calculated. Reception Hoyle s Fallacy is rejected by evolutionary ... more details
Protoporphyrins are tetrapyrroles containing the following side chain s methyl 4 propionic acid 2 vinyl 2 Protoporphyrin IX is a biochemically widely used carrier molecule for divalent cations. Together with iron Fe 2 the body of the heme group of hemoglobin , myoglobin and many other heme containing enzymes like cytochrome c and catalase are formed. Complexed with magnesium ions Mg 2 the main part of the Chlorophylls are formed. Complexed with zinc ions Zn 2 it forms Zinc protoporphyrin . The number e.g. IX indicates the position of different side chains, but historically, as the nomenclature has grown, it has done so systematically only in parts. Protoporphyrin IX as a direct precursor of heme is accumulated by patients of erythropoietic protoporphyria , which is one of the genetic disorders of the biosynthesis of the heme pathway. It causes a severe photosensivity against visible light. The sensitivity of protoporphyrin IX against light is also used as a therapy against different forms of cancer photodynamic therapy , PDT . Protoporphyrins are deposited in the shells of the egg biology eggs of some bird s as a brown or red pigment, either as a ground colour or as spotting. This occurs in most passerine species, some ground nesting non passerines, such as wader s, gull s, nightjar s and sandgrouse , where it provides camouflage, and some brood parasite parasitic cuckoo s, which need to mimic their passerine hosts eggs. Protoporphyrins strengthen the egg shell, and are deposited where the shell is too thin as a result of calcium shortage. Spotting therefore tend to be heavier where the local soil is calcium deficient, and in the eggs laid last in a clutch. External links MeshName Protoporphyrins PubChem 4971 protoporphyrin IX Tetrapyrroles biochem stub Category Tetrapyrroles fr Protoporphyrine it Protoporfirina nl Protoporfyrine ja ... more details
Automatic taxobox binomial Borrelia anserina binomial authority Sakharoff 1891 Bergey et al. 1925 Borrelia anserina is a helical filiform spirochete bacteria with dimensions of approximately 8 20 0,2 0,3 Micrometre m and with about 5 to 8 spirals. Their mobility is very high. B. anserina can be colored with the May Grunwald Giemsa method . ref name Diurpaneu cite book author Gheorghe Rapunteanu, Sorin Rapunteanu editors title Bacteriologie Veterinara Speciala edition I publisher Editura AcademicPress, Cluj Napoca, Romania year 2005 id ISBN 973 7950 95 X ref Cultivation In Microbiological laboratories, B. anserina bacteria can be grown on special protein enriched mediums rich in ovoalbumins or animal tissue that contains Myoglobin , in wikt anaerobic anaerobic conditions. They can also be grown in embrionated chicken eggs. The laboratory cultivation of B. anserina is rarely done and constitutes a diagnostic method in bird borreliosis and spirochetosis. ref name Diurpaneu Pathogenity B. anserina is a pathogenic agent for birds chickens, turkeys, ducks etc. and causes a disease called borreliosis or spirochetosis . This bacteria is transmitted from bird to bird by ticks from the Argas and Ornitodorus genus. The major symptoms of an infection with B. anserina are anemia , diarrhea and severe neurological dysfunctions. Image Argastick.jpg thumb These two ticks represent the Argasidae soft ticks Lt , and the Ixodidae hard ticks References references External links http www.pubmedcentral.nih.gov articlerender.fcgi?artid 385494 A STUDY OF BORRELIA ANSERINA INFECTION SPIROCHETOSIS IN TURKEYS Category Poultry diseases veterinary med stub bacteria stub es Borrelia anserina fr Borrelia anserina ... more details
saved book title Biochemistry subtitle An introduction cover image AminoAcidball.svg cover color black Biochemistry An introduction This collection of Wikipedia articles is intended to supplement a standard textbook of biochemistry. Students may find its explanations complement their texts for greater clarity. In some areas its information will extend past their texts. In a few areas, information is still lacking but students are warmly welcomed to make up that deficit Cells and water Biochemistry Cell biology Cells Water Structural Biochemistry Nucleic acids Nucleic acid RNA DNA Proteins and amino acids Protein Amino acid Proteinogenic amino acid Properties of the twenty amino acids Myoglobin Hemoglobin Enzyme mechanisms Enzyme catalysis Enzyme kinetics Enzyme kinetics Lipids and membranes Lipid Biological membrane Membrane protein Cell membrane Carbohydrate structure Carbohydrate Polysaccharide Intermediary metabolism Metabolism Metabolism Overview of metabolism Carbohydrate metabolism Glycolysis Gluconeogenesis Glycogen Pentose phosphate pathway Citric acid cycle Citric acid cycle Oxidative phosphorylation Oxidative phosphorylation Photosynthesis Photosynthesis Lipid metabolism Fatty acid synthesis Lipogenesis Acetyl CoA carboxylase Fatty acid degradation Beta oxidation Nitrogen metabolism Nitrogen fixation Amino acid synthesis Nucleotide Urea cycle Integration of metabolism Hormone Signal transduction Diabetes mellitus Informational Macromolecules DNA synthesis and repair DNA replication DNA repair Oncogene Oncogenes RNA synthesis and processing Transcription genetics Transcription Regulation of gene expression Protein synthesis and modifications Translation biology Translation Posttranslational modification Proteolysis Proteasome Category Wikipedia books on biology Biochemistry an introduction Category Wikipedia books on chemistry Biochemistry an introduction ... more details
orphan date August 2009 Meat emulsion is a two phase system, with the dispersed phase consisting of either solid or liquid fat particles and the continuous phase being the water containing salts and dissolved, gelled and suspended proteins . Thus they can be classified as oil in water emulsion. Meat emulsion is not a true emulsion since the two phases involved are not liquids and the fat droplets in a commercial emulsion are larger than 50 m in diameter and thus do not conform to one of the requirement of a classical emulsion. The continuous phase mainly consists of water, water soluble proteins and salt soluble proteins. The dispersed phase or discontinuous phase consists of fat droplets. The water soluble proteins are sarcoplasm sarcoplasmic proteins such as myoglobin and other pigment s, salt soluble proteins are myofibrillar proteins such as myosin , actin , and actinin s. clarify this sentence doesn t make sense as written date September 2011 Meat emulsifiers When used in food products, iota carrageenan and sodium stearoyl lactylate SSL have a synergistic effect allowing for stabilizing emulsifying that is not obtained with any other type of carrageenan kappa lambda or with other emulsifiers monoglyceride s, etc. . Sodium stearoyl lactylate combined with iota carrageenan is capable of producing emulsions under both hot and cold conditions using either vegetable or animal fat. References Principles of Meat Science by Elton D. Aberle, John C. Forrest, David E. Gerrard, Edward W. Mills, Harold B. Hedrick, Max D. Judge, Robert A. Merkel DEFAULTSORT Meat Emulsion Category Meat ... more details
which is likewise very similar to multiple subunits of myoglobin and it contains many 16 17 kDa myoglobin like subunits arranged in a giant complex of over a hundred subunits with interlinking proteins ... more details
of myoglobin , allowing the muscle to use oxygen more efficiently for aerobic respiration . In contrast ... which requires little of the meat darkening myoglobin. Note that this holds for ground based birds ... more details
Infobox Disease Name PAGENAME Image Caption DiseasesDB 13135 ICD10 ICD10 T 79 5 t 79 ICD9 ICD9 958.5 ICDO OMIM MedlinePlus eMedicineSubj eMedicineTopic MeshID D003444 Crush syndrome also physical trauma traumatic rhabdomyolysis or Bywaters syndrome is a medical condition characterized by major Shock medical shock and renal failure after a wikt crush crushing injury to skeletal muscle . Cases occur commonly in catastrophes such as earthquake s, in which victims that have been trapped under fallen masonry. Pathophysiology The syndrome was discovered by United Kingdom British physician Eric Bywaters in patients during the 1941 London The Blitz Blitz . ref WhoNamedIt synd 3870 ref ref cite journal last Bywaters first E. G. last2 Beall first2 D. title Crush injuries with impairment of renal function journal British Medical Journal Br Med J year 1941 volume 1 issue pages 427 432 doi ref It is a reperfusion injury that appears after the release of the crushing pressure. The mechanism is believed to be the release into the bloodstream of muscle breakdown products notably myoglobin , potassium and phosphorus that are the products of rhabdomyolysis the breakdown of skeletal muscle damaged by ischemia ischemic conditions . The specific action on the kidney s is not understood completely, but may be due partly to nephrotoxicity nephrotoxic metabolite s of myoglobin. Seigo Minami , a Japanese physician, first reported the crush syndrome in 1923. ref cite journal last Minami first Seigo year 1923 title ber Nierenver nderungen nach Versch ttung journal Virchows Arch. Patho. Anat. volume 245 issue 1 pages doi 10.1007 BF01992107 ref ref Medical discoveries Who and when Schmidt JF. Springfield CC Thomas, 1959. p.115. ref ref Morton s medical bibliography An annotated check list of texts illustrating History of medicine Garrison Morton . Aldershot Solar Press 1911. p.654. ref He studied the pathology of three soldiers who died in World War I from insufficiency of the kidney. The rena ... more details
James P. Collman born 1932 in Beatrice, Nebraska is an American Professor of Chemistry. He is currently serving at Stanford University in California. Collman is considered a pioneer in bioinorganic and biomimetic chemistry. He developed a clearer understanding of the mechanisms of biological proteins, by studying synthetic analogs of biological systems which contain metal and metalloid atoms. His work on hemoglobin, myoglobin and cytochrome c oxidase allowed subsequent researchers to understand how the protein metal interactions allow these molecules to function. ref Chemical & Engineering News , 19 January 2009, p. 73 ref Career Collman received B.S. 1954 and M.S. degrees 1956 in Chemistry from the University of Nebraska Lincoln . He received a Ph.D. degree from the University of Illinois at Urbana Champaign in 1958 under Reynold C. Fuson . Upon receiving his Ph. D., Collman joined the faculty of University of North Carolina at Chapel Hill , remaining there until 1967, when he moved to Stanford University. He currently holds the George & Hilda M. Daubert Endowed Chair in Chemistry at Stanford. Collman has contributed to several aspects of transition metal chemistry. He has authored 3 books and over 366 Academic publishing scientific papers . In the 1960s his group demonstrated that certain metal acetylacetonate s undergo Friedel Crafts like reactions, indicating that these chelate rings have aromatic character. Through reviews as well as original research, his group popularized the oxidative addition reaction, leading to the discovery of new low valent complexes including Ru CO sub 3 sub PPh sub 3 sub sub 2 sub and IrCl N sub 2 sub PPh sub 3 sub sub 2 sub . Collman s reagent , Na sub 2 sub Fe CO sub 4 sub , prepared in his laboratories, enables certain C C coupling reactions in organic synthesis . He popularized the use of tetraphenylporphyrin as a Biomimicry biomimetic Ligand biochemistry ligand for exploring the structure and function of myoglobin , cytochrome P4 ... more details
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